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Large-scale Proteomic and Phosphoproteomic Analyses of Maize Seedling Leaves During De-etiolation

文献类型： 外文期刊

作者： Gao, Zhi-Fang 1 ; Shen, Zhuo 2 ; Chao, Qing 1 ; Yan, Zhen 1 ; Ge, Xuan-Liang 3 ; Lu, Tiancong 4 ; Zheng, Haiyan 5 ; Qian, Chun-Rong 3 ; Wang, Bai-Chen 1 ;

作者机构： 1.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, CAS, Beijing 100093, Peoples R China

2.Guangdong Acad Agr Sci, Vegetable Res Inst, Guangdong Key Lab New Technol Res Vegetables, Guangzhou 510640, Peoples R China

3.Heilongjiang Acad Agr Sci, Inst Crop Cultivat & Farming, Harbin 150086, Peoples R China

4.Beijing Prot World Biotech, Beijing 100012, Peoples R China

5.Rutgers State Univ, Ctr Adv Biotechnol & Med, Biol Mass Spectrometry Facil, Piscataway, NJ 08855 USA

6.Univ Chinese Acad Sci, Beijing 100049, Peoples R China

关键词： Maize seedling leaves; De-etiolation; Quantitative analysis; Proteome; Phosphoproteome

期刊名称：GENOMICS PROTEOMICS & BIOINFORMATICS （ 影响因子：6.409； 五年影响因子：10.196 ）

ISSN： 1672-0229

年卷期： 2020 年 18 卷 4 期

页码：

收录情况： SCI

摘要： De-etiolation consists of a series of developmental and physiological changes that a plant undergoes in response to light. During this process light, an important environmental signal, triggers the inhibition of mesocotyl elongation and the production of photosynthetically active chloroplasts, and etiolated leaves transition from the "sink" stage to the "source" stage. De-etiolation has been extensively studied in maize (Zea mays L.). However, little is known about how this transition is regulated. In this study, we described a quantitative proteomic and phosphoproteomic atlas of the de-etiolation process in maize. We identified 16,420 proteins in proteome, among which 14,168 proteins were quantified. In addition, 8746 phosphorylation sites within 3110 proteins were identified. From the combined proteomic and phosphoproteomic data, we identified a total of 17,436 proteins. Only 7.0% (998/14,168) of proteins significantly changed in abundance during de-etiolation. In contrast, 26.6% of phosphorylated proteins exhibited significant changes in phosphorylation level; these included proteins involved in gene expression and homeostatic pathways and rate-limiting enzymes involved in photosynthetic light and carbon reactions. Based on phosphoproteomic analysis, 34.0% (1057/3110) of phosphorylated proteins identified in this study contained more than 2 phosphorylation sites, and 37 proteins contained more than 16 phosphorylation sites, indicating that multi-phosphorylation is ubiquitous during the de-etiolation process. Our results suggest that plants might preferentially regulate the level of posttranslational modifications (PTMs) rather than protein abundance for adapting to changing environments. The study of PTMs could thus better reveal the regulation of de-etiolation.

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